SRPK1

Summary

SRPK1 (SRSF protein kinase 1, HGNC:11305) is a protein-coding gene on chromosome 6p21.31, encoding SRSF protein kinase 1 (Q96SB4). Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicin….

This gene encodes a serine/arginine protein kinase specific for the SR (serine/arginine-rich domain) family of splicing factors. The protein localizes to the nucleus and the cytoplasm. It is thought to play a role in regulation of both constitutive and alternative splicing by regulating intracellular localization of splicing factors. Alternative splicing of this gene results in multiple transcript variants. Additional alternatively spliced transcript variants have been described for this gene, but their full length nature have not been determined.

Source: NCBI Gene 6732 — RefSeq curated summary.

At a glance

• GWAS associations: 4
• Clinical variants (ClinVar): 83 total
• Druggable target: yes — 24 molecules with ChEMBL bioactivity
• MANE Select transcript: NM_003137

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:11305
Approved symbol	SRPK1
Name	SRSF protein kinase 1
Location	6p21.31
Locus type	gene with protein product
Status	Approved
Aliases	SFRSK1
Ensembl gene	ENSG00000096063
Ensembl biotype	protein_coding
OMIM	601939
Entrez	6732

Gene structure

Transcript identifiers

Ensembl transcripts: 22 — 15 protein_coding, 4 retained_intron, 2 nonsense_mediated_decay, 1 protein_coding_CDS_not_defined

ENST00000346162, ENST00000361690, ENST00000373821, ENST00000373825, ENST00000423325, ENST00000502969, ENST00000505885, ENST00000507292, ENST00000507909, ENST00000508473, ENST00000510290, ENST00000512445, ENST00000513367, ENST00000876560, ENST00000876561, ENST00000876562, ENST00000876563, ENST00000926028, ENST00000926029, ENST00000926030, ENST00000952658, ENST00000952659

RefSeq mRNA: 1 — MANE Select: NM_003137 NM_003137

CCDS: CCDS47415

Canonical transcript exons

ENST00000373825 — 16 exons

Exon	Start	End
ENSE00002026764	35832966	35835488
ENSE00003469810	35920468	35920528
ENSE00003505348	35872563	35872728
ENSE00003510963	35857261	35857368
ENSE00003528224	35870934	35870959
ENSE00003547876	35870281	35870494
ENSE00003590934	35921044	35921098
ENSE00003596236	35886724	35886811
ENSE00003636247	35842535	35842604
ENSE00003638466	35838337	35838429
ENSE00003647176	35869482	35869901
ENSE00003655779	35874233	35874339
ENSE00003660994	35869010	35869110
ENSE00003669405	35888815	35888923
ENSE00003684043	35890895	35891013
ENSE00003737915	35888024	35888111

Expression profiles

Bgee: expression breadth ubiquitous, 289 present calls, max score 96.46.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 47.8840 / max 914.1612, expressed in 1818 samples.

FANTOM5 promoters (3 alternative TSS)

Promoter ID	TPM avg	Samples expressed
73329	39.4956	1816
73328	7.4942	1678
73330	0.8941	568

Top tissues by expression

295 total, by Bgee expression score (0-100, higher = more expressed):

Tissue	Anatomy ID	Expression score	Quality
sperm	CL:0000019	96.46	gold quality
cartilage tissue	UBERON:0002418	96.09	gold quality
colonic epithelium	UBERON:0000397	96.00	gold quality
trabecular bone tissue	UBERON:0002483	95.62	gold quality
cervix squamous epithelium	UBERON:0006922	95.59	gold quality
bone marrow	UBERON:0002371	94.90	gold quality
upper leg skin	UBERON:0004262	94.80	gold quality
secondary oocyte	CL:0000655	94.61	gold quality
endothelial cell	CL:0000115	94.59	gold quality
mucosa of sigmoid colon	UBERON:0004993	94.56	gold quality
blood	UBERON:0000178	94.44	gold quality
bone marrow cell	CL:0002092	94.36	gold quality
colonic mucosa	UBERON:0000317	94.32	gold quality
male germ cell	CL:0000015	94.16	gold quality
penis	UBERON:0000989	94.15	gold quality
male germ line stem cell (sensu Vertebrata) in testis	CL:0000089 ∩ UBERON:0000473	94.07	gold quality
rectum	UBERON:0001052	94.04	gold quality
cortical plate	UBERON:0005343	93.95	gold quality
tonsil	UBERON:0002372	93.51	gold quality
oocyte	CL:0000023	93.05	gold quality
mammalian vulva	UBERON:0000997	92.95	gold quality
pigmented layer of retina	UBERON:0001782	92.34	gold quality
pharyngeal mucosa	UBERON:0000355	92.04	gold quality
primordial germ cell in gonad	CL:0000670 ∩ UBERON:0000991	91.94	gold quality
squamous epithelium	UBERON:0006914	91.94	gold quality
duodenum	UBERON:0002114	91.80	gold quality
gingival epithelium	UBERON:0001949	91.77	gold quality
cervix epithelium	UBERON:0004801	91.51	gold quality
jejunal mucosa	UBERON:0000399	91.41	gold quality
ganglionic eminence	UBERON:0004023	91.30	gold quality

Single-cell (SCXA)

Detected in 2 experiment(s), a significant marker in 2.

Experiment	Marker?	Max mean expression
E-MTAB-8410	yes	392.39
E-ANND-3	yes	11.37

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): WT1

miRNA regulators (miRDB)

158 targeting SRPK1, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNA	Max score	Avg score	miRNA target_count
HSA-MIR-1252-5P	100.00	69.80	2774
HSA-MIR-5196-5P	100.00	67.98	2761
HSA-MIR-4747-5P	100.00	67.90	2681
HSA-MIR-3646	100.00	73.56	5283
HSA-MIR-5692A	100.00	74.40	6850
HSA-MIR-3613-3P	100.00	76.36	7965
HSA-MIR-9-5P	100.00	72.28	2361
HSA-MIR-186-5P	99.99	70.83	3707
HSA-MIR-548C-3P	99.99	74.01	7587
HSA-MIR-6077	99.99	68.04	2299
HSA-MIR-3692-3P	99.98	70.27	2139
HSA-MIR-520D-5P	99.98	73.34	4883
HSA-MIR-524-5P	99.98	73.43	4882
HSA-MIR-3148	99.97	75.06	6478
HSA-MIR-493-5P	99.96	72.47	2382
HSA-MIR-570-3P	99.96	72.41	4910
HSA-MIR-23A-3P	99.95	74.24	3163
HSA-MIR-23B-3P	99.95	74.24	3163
HSA-MIR-23C	99.95	73.92	3192
HSA-MIR-6508-5P	99.92	70.67	2465
HSA-MIR-497-5P	99.92	71.83	2674
HSA-MIR-5680	99.91	69.83	3421
HSA-MIR-15A-5P	99.90	72.80	2787
HSA-MIR-15B-5P	99.90	72.78	2798
HSA-MIR-16-5P	99.90	72.80	2780
HSA-MIR-195-5P	99.90	72.81	2805
HSA-MIR-106A-5P	99.90	73.94	2683
HSA-MIR-627-3P	99.90	71.42	3316
HSA-MIR-345-3P	99.89	70.23	1421
HSA-MIR-17-5P	99.89	73.83	2665

Literature-anchored findings (GeneRIF, showing 40)

• Both SRPK1 and SRPK2 are most likely the cellular protein kinases mediating HBV core protein phosphorylation during viral infection and therefore represent important host cell targets for therapeutic intervention in HBV infection. (PMID:12134018)
• negative role of SRPK1 and SRPK2 in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein (PMID:16122776)
• ASF/SF2 is phosphorylated by SRPK1 and Clk/Sty (PMID:16223727)
• We describe crystallographic, molecular dynamics, and biochemical results that shed light on how SRPK1 preserves its constitutive active conformation. (PMID:17223538)
• Serine-arginine protein kinase 1 overexpression is associated with tumorigenic imbalance in mitogen-activated protein kinase pathways. (PMID:17332336)
• SRPK1 binding is associated with phosphorylation of human papillomavirus type 1 E1/E4 polypeptide and modulates autophosphorylation of the kinase. (PMID:17360743)
• Sky1p utilizes the same docking groove to bind yeast SR-like protein Gbp2p and phosphorylates all three serines present in a contiguous RS dipeptide stretch (PMID:17517895)
• These studies reveal that SRPK1 docks near the C-terminus of the RS1 segment of ASF protein and then moves in an N-terminal direction along the RS domain. (PMID:18155240)
• Data show that a sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1. (PMID:18342604)
• Data show that adaptable molecular interactions guide phosphorylation of the SR protein ASF/SF2 by SRPK1. (PMID:18687337)
• SRPK1, a ubiquitously expressed SR protein-specific kinase, directly binds to the cochaperones Hsp40/DNAjc8 and Aha1, which mediate dynamic interactions of the kinase with the major molecular chaperones Hsp70 and Hsp90 in mammalian cells (PMID:19240134)
• while local RS/SR content steers regional preferences in the RS domain, distal contacts with SRPK1 guide initiation and directional phosphorylation within these regions. (PMID:19477182)
• These results indicate that ICP27 RGG box methylation regulates interaction ALY and SRPK1 proteins. (PMID:19553338)
• The enzymatic activity of SR protein kinases 1 and 1a is negatively affected by interaction with scaffold attachment factors B1 and 2. (PMID:19674106)
• Our results demonstrate that SRPK1 and SRPK2 are host factors essential for Hepatitis C virus replication. (PMID:20498328)
• SRPK1a may play an important role in linking ribosomal assembly and/or function to erythroid differentiation in human leukaemic cells (PMID:20708644)
• protein kinase SRPK1 phosphorylates ~10 serines in the arginine–serine-rich domain (RS domain) of the SR protein SRSF1 in a C- to N-terminal direction, a modification that directs this essential splicing factor from the cytoplasm to the nucleus (PMID:21728354)
• The present immunohistochemical study reveals a region- and neuron-specific localization of SRPK1 in human brain. (PMID:22019390)
• WT1 bound to the SRPK1 promoter, and repressed expression through a specific WT1 binding site (PMID:22172722)
• These findings reveal a major signal transduction pathway for regulated splicing and place SRPKs in a central position in the pathway, consistent with their reputed roles in a large number of human cancers. (PMID:22727668)
• positively regulates IFN-lambda1 genes during viral infection (PMID:23405030)
• SRPK1 plays an oncogenic role in hepatocellular carcinoma through a possible mechanism involving PI3K/Akt. (PMID:23644876)
• The data establish a new view of SRSF1 protein regulation in which SRPK1 and CLK1 partition activities based on Ser-Pro versus Arg-Ser placement rather than on N- and C-terminal preferences along the RS domain. (PMID:23707382)
• Data suggest that the conformation of SRPK1 is highly flexible and can readily adapt to changes in structure of arginine-serine rich domains in substrate proteins such as SRSF1 (serine-arginine-rich splicing protein 1). (PMID:24074032)
• Increased expression of SRPK1 correlates with the progression of breast cancer.SRPK1 is upregulated in breast cancer at both mRNA and protein levels. (PMID:24961466)
• The data show that the RS domain in SRSF1 is multifunctional and that sequences once thought to be catalytically silent can be recruited to enhance the efficiency of SR protein phosphorylation. (PMID:24984036)
• Hypoxic stress decreased the miR-9 level in ARPE-19 cells, which increased the transcriptional level of SRPK-1, resulting in alternative splicing shift to pro-angiogenic isoforms of VEGF165 in human retinal pigment epithelial cells. (PMID:25007957)
• Inhibition of SRPK1 by knockdown or with pharmacological inhibitors reduces expression of pro-angiogenic forms of VEGF. (PMID:25010863)
• Up-regulation of SRPK1 is associated with breast cancer. (PMID:25140042)
• Collectively, these data suggest that human papillomavirus type 1 E1;E4-mediated inhibition of SRPK1 could affect the functions of host serine-arginine proteins and those of the virus transcription/replication regulator E2. (PMID:25142587)
• Authors show that MNK regulates SRPK via mTOR and AKT. (PMID:25187540)
• ERK1/2 signal induced MNK catalytic activity enabled enterovirus type 1 internal ribosomal entry site-mediated translation/host cell cytotoxicity through negative regulation of the Ser/Arg (SR)-rich protein kinase (SRPK). (PMID:25187541)
• Modulation of SRPK1 and subsequent inhibition of tumour angiogenesis. (PMID:25381816)
• Data suggest that proline phosphorylation by CLK1/CDC-like kinase 1 (but not by SRPK1/serine/arginine-rich splicing factor kinase 1) regulates conformation and alternative splicing function of SFRS1 (serine/arginine-rich splicing factor 1). (PMID:25529026)
• SRPK1 was highly expressed in basal breast cancer. High SRPK1 expression correlated with poor breast cancer disease outcome and preferential metastasis to the lungs and brain. (PMID:25774502)
• SRPK1 may be a potential anticancer target to inhibit glioma progression. (PMID:25833691)
• SRPK1 is a regulator of Tra2beta1 splicing function and individual domains engage in considerable cross-talk, assuming novel functions with regard to RNA binding, splicing, and catalysis. (PMID:26013829)
• SRPK1 mediates TGF-beta-induced proliferation. (PMID:26099172)
• SRPK1 is overexpressed in HCC and may be a promising indicator of prognosis for HCC patients (PMID:26201897)
• Data indicate serine/arginine-rich protein kinases SRPK1/2/SRPIN340 complexes by molecular docking and molecular dynamics. (PMID:26244849)

Cross-species orthologs

12 orthologs

Organism	Symbol	Gene ID
danio_rerio	srpk1b	ENSDARG00000031560
mus_musculus	Srpk1	ENSMUSG00000004865
rattus_norvegicus	Srpk1	ENSRNOG00000000511
drosophila_melanogaster	CG8565	FBGN0030697
drosophila_melanogaster	SRPK	FBGN0286813
caenorhabditis_elegans		WBGENE00002187
caenorhabditis_elegans		WBGENE00002188
caenorhabditis_elegans		WBGENE00004055
caenorhabditis_elegans		WBGENE00004056
caenorhabditis_elegans		WBGENE00004980
caenorhabditis_elegans	gskl-2	WBGENE00007977
caenorhabditis_elegans	Y106G6E.1	WBGENE00013705

Paralogs (19): MAPK9 (ENSG00000050748), MAPK6 (ENSG00000069956), MOK (ENSG00000080823), NLK (ENSG00000087095), MAPK1 (ENSG00000100030), MAPK3 (ENSG00000102882), MAPK8 (ENSG00000107643), MAPK10 (ENSG00000109339), MAK (ENSG00000111837), MAPK14 (ENSG00000112062), CILK1 (ENSG00000112144), SRPK2 (ENSG00000135250), MAPK4 (ENSG00000141639), MAPK13 (ENSG00000156711), MAPK7 (ENSG00000166484), MAPK15 (ENSG00000181085), SRPK3 (ENSG00000184343), MAPK11 (ENSG00000185386), MAPK12 (ENSG00000188130)

Protein

Protein identifiers

SRSF protein kinase 1 — Q96SB4 (reviewed: Q96SB4)

Alternative names: SFRS protein kinase 1, Serine/arginine-rich protein-specific kinase 1

All UniProt accessions (7): Q96SB4, D6RB98, D6RBF8, D6RBM8, D6RDZ3, H0Y932, H3BLV9

UniProt curated annotations — full annotation on UniProt →

Function. Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation. Phosphorylates the N-terminus of ERC1.

Subunit / interactions. Monomer. Isoform 2 is found in a multisubunit complex containing seven proteins, named toposome, which separates entangled circular chromatin DNA during chromosome segregation. Isoform 2 interacts with DNAJC8 and AHSA1/AHA1 and this mediates formation of a complex with the Hsp70 /Hsp90 machinery. Isoform 1 is found in a complex with: DHX9, MOV10, MATR3, HNRNPU, NCL, DDX21, HSD17B4, PABPC1, HNRNPM, IGF2BP1, SYNCRIP, RPL3, VIM, YBX1, NPM1, HNRNPA2B1, HNRNPC, RPLP0, RPL7A and RALY. Isoform 2 binds to IGF2BP1, SYNCRIP, HNRNPA2B1 and HNRNPC. Isoform 1 and isoform 2 interact with SAFB which inhibits its activity. Isoform 2 interacts with SAFB2 which inhibits its activity. Interacts (via kinase domain) with ERC1 (via N-terminus); the interaction is direct and may be involved in SRPK protein localization. (Microbial infection) Isoform 2 interacts with HHV-1 ICP27 protein.

Subcellular location. Cytoplasm. Nucleus. Nucleus matrix. Microsome Cytoplasm. Nucleoplasm. Nucleus speckle. Chromosome.

Tissue specificity. Isoform 2 is predominantly expressed in the testis but is also present at lower levels in heart, ovary, small intestine, liver, kidney, pancreas and skeletal muscle. Isoform 1 is only seen in the testis, at lower levels than isoform 2. Highly expressed in different erythroid and lymphoid cell lines, with isoform 2 being far more abundant than isoform 1.

Activity regulation. Activated by phosphorylation on Ser-51 and Ser-555.

Miscellaneous. Due to intron retention.

Similarity. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family.

Isoforms (3)

UniProt ID	Names	Canonical?
Q96SB4-2	2	yes
Q96SB4-3	1, 1a
Q96SB4-4	3

RefSeq proteins (1): NP_003128* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR000719	Prot_kinase_dom	Domain
IPR008271	Ser/Thr_kinase_AS	Active_site
IPR011009	Kinase-like_dom_sf	Homologous_superfamily
IPR017441	Protein_kinase_ATP_BS	Binding_site
IPR051334

Pfam: PF00069

Catalyzed reactions (Rhea), 2 shown:

• L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+) (RHEA:17989)
• L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+) (RHEA:46608)

UniProt features (68 total): helix 21, strand 10, mutagenesis site 7, modified residue 5, compositionally biased region 5, sequence conflict 4, turn 4, binding site 3, region of interest 3, splice variant 2, chain 1, domain 1, active site 1, sequence variant 1

Structure

Experimental structures (PDB)

12 structures.

PDB	Method	Resolution (Å)
5NNG	X-RAY DIFFRACTION	1.2
5MY8	X-RAY DIFFRACTION	1.7
1WAK	X-RAY DIFFRACTION	1.73
5MXX	X-RAY DIFFRACTION	1.75
4WUA	X-RAY DIFFRACTION	2
7DD1	X-RAY DIFFRACTION	2.05
7PQS	X-RAY DIFFRACTION	2.2
7ZKS	X-RAY DIFFRACTION	2.28
5XV7	X-RAY DIFFRACTION	2.32
1WBP	X-RAY DIFFRACTION	2.4
6FAD	X-RAY DIFFRACTION	2.8
3BEG	X-RAY DIFFRACTION	2.9

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-Q96SB4-F1	71.65	0.51

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Catalytic / active sites (1): 213 (proton acceptor)

Ligand- & substrate-binding residues (3): 86–94; 109; 166–168

Post-translational modifications (5): 51, 309, 311, 333, 555

Mutagenesis-validated functional residues (7):

Position	Phenotype
37	no effect on protein phosphorylation.
51	protein phosphorylation impaired at this position.
222	no effect on protein phosphorylation.
311	no effect on protein phosphorylation.
436	no effect on protein phosphorylation.
555	protein phosphorylation impaired at this position.
619	no effect on protein phosphorylation.

Function

Pathways and Gene Ontology

Reactome pathways

11 pathways

ID	Pathway
R-HSA-9694631	Maturation of nucleoprotein
R-HSA-9821993	Replacement of protamines by nucleosomes in the male pronucleus
R-HSA-1266738	Developmental Biology
R-HSA-1643685	Disease
R-HSA-5663205	Infectious disease
R-HSA-9679506	SARS-CoV Infections
R-HSA-9694516	SARS-CoV-2 Infection
R-HSA-9694635	Translation of Structural Proteins
R-HSA-9772573	Late SARS-CoV-2 Infection Events
R-HSA-9816359	Maternal to zygotic transition (MZT)
R-HSA-9824446	Viral Infection Pathways

MSigDB gene sets: 278 (showing top): MORF_DNMT1, MODULE_52, BORCZUK_MALIGNANT_MESOTHELIOMA_UP, RODRIGUES_THYROID_CARCINOMA_ANAPLASTIC_UP, AAGCAAT_MIR137, TGCGCANK_UNKNOWN, MORF_BUB1, TGCTGCT_MIR15A_MIR16_MIR15B_MIR195_MIR424_MIR497, GOBP_NEGATIVE_REGULATION_OF_VIRAL_PROCESS, GOBP_POSITIVE_REGULATION_OF_VIRAL_GENOME_REPLICATION, SHAFFER_IRF4_TARGETS_IN_ACTIVATED_B_LYMPHOCYTE, GOBP_MALE_GAMETE_GENERATION, TTGCWCAAY_CEBPB_02, CEBPB_01, OUELLET_OVARIAN_CANCER_INVASIVE_VS_LMP_UP

GO Biological Process (13): spliceosomal complex assembly (GO:0000245), protein phosphorylation (GO:0006468), chromosome segregation (GO:0007059), RNA splicing (GO:0008380), sperm DNA condensation (GO:0035092), intracellular signal transduction (GO:0035556), positive regulation of viral genome replication (GO:0045070), negative regulation of viral genome replication (GO:0045071), innate immune response (GO:0045087), regulation of mRNA splicing, via spliceosome (GO:0048024), regulation of mRNA processing (GO:0050684), mRNA processing (GO:0006397), cell differentiation (GO:0030154)

GO Molecular Function (10): magnesium ion binding (GO:0000287), RNA binding (GO:0003723), protein kinase activity (GO:0004672), protein serine/threonine kinase activity (GO:0004674), ATP binding (GO:0005524), protein serine kinase activity (GO:0106310), nucleotide binding (GO:0000166), protein binding (GO:0005515), kinase activity (GO:0016301), transferase activity (GO:0016740)

GO Cellular Component (10): chromatin (GO:0000785), nucleus (GO:0005634), nucleoplasm (GO:0005654), cytoplasm (GO:0005737), cytosol (GO:0005829), plasma membrane (GO:0005886), nuclear matrix (GO:0016363), nuclear speck (GO:0016607), chromosome (GO:0005694), endoplasmic reticulum (GO:0005783)

Reactome top-level categories

Rollup of top-9 pathways:

Category	Pathways
Translation of Structural Proteins	1
Maternal to zygotic transition (MZT)	1
Disease	1
Viral Infection Pathways	1
SARS-CoV Infections	1
Late SARS-CoV-2 Infection Events	1
SARS-CoV-2 Infection	1
Developmental Biology	1
Infectious disease	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
cellular anatomical structure	5
mRNA splicing, via spliceosome	2
RNA processing	2
intracellular anatomical structure	2
viral genome replication	2
regulation of viral genome replication	2
protein kinase activity	2
intracellular membrane-bounded organelle	2
nuclear lumen	2
cytoplasm	2
protein-RNA complex assembly	1
phosphorylation	1
protein modification process	1
cell cycle process	1
chromatin organization	1
spermatid nucleus differentiation	1
signal transduction	1
positive regulation of viral process	1
negative regulation of viral process	1
immune response	1
defense response to symbiont	1
regulation of RNA splicing	1
regulation of mRNA processing	1
mRNA processing	1
regulation of mRNA metabolic process	1
mRNA metabolic process	1
cellular developmental process	1
metal ion binding	1
nucleic acid binding	1
kinase activity	1
phosphotransferase activity, alcohol group as acceptor	1
catalytic activity, acting on a protein	1
adenyl ribonucleotide binding	1
purine ribonucleoside triphosphate binding	1
nucleoside phosphate binding	1
heterocyclic compound binding	1
binding	1
transferase activity, transferring phosphorus-containing groups	1
catalytic activity	1
chromosome	1

Protein interactions and networks

STRING

2774 interactions, top by confidence (×1000):

Protein A	Protein B	Partner UniProt	Score
SRPK1	SRSF1	Q07955	949
SRPK1	DDX23	Q9BUQ8	922
SRPK1	SRSF2	Q01130	881
SRPK1	HNRNPC	P07910	775
SRPK1	HSPA4	P34932	770
SRPK1	SRSF5	Q13243	770
SRPK1	DHX9	Q08211	730
SRPK1	DDX21	Q9NR30	721
SRPK1	AHSA1	O95433	717
SRPK1	SRSF9	Q13242	701
SRPK1	SRSF6	Q13247	685
SRPK1	LUC7L3	O95232	684
SRPK1	DNAJB1	P25685	681
SRPK1	SNRNP70	P08621	678
SRPK1	TRA2B	P62995	669

IntAct

384 interactions, top by confidence:

A	B	Type	Score
RNPS1	SRPK1	psi-mi:“MI:0915”(physical association)	0.840
SRPK1	RNPS1	psi-mi:“MI:0915”(physical association)	0.840
DDX21	HNRNPC	psi-mi:“MI:0915”(physical association)	0.750
SRPK1	N	psi-mi:“MI:0217”(phosphorylation reaction)	0.710
SRPK1	N	psi-mi:“MI:0407”(direct interaction)	0.710
SNRPD2	GEMIN2	psi-mi:“MI:0914”(association)	0.710
PTK2	TGFB1I1	psi-mi:“MI:0914”(association)	0.680
U2AF1	U2AF2	psi-mi:“MI:0914”(association)	0.670
SRSF1	SRPK1	psi-mi:“MI:0915”(physical association)	0.670
SRPK1	SRSF1	psi-mi:“MI:0915”(physical association)	0.670
DGCR8	SRPK1	psi-mi:“MI:0915”(physical association)	0.670
DHX8	AHCYL1	psi-mi:“MI:0914”(association)	0.640
SNRNP70	GEMIN2	psi-mi:“MI:0914”(association)	0.640
SRPK1	SNRPC	psi-mi:“MI:0914”(association)	0.640
SRPK1	YTHDC1	psi-mi:“MI:0915”(physical association)	0.570
YTHDC1	SRPK1	psi-mi:“MI:0915”(physical association)	0.570
SRPK1	SNRPD3	psi-mi:“MI:0915”(physical association)	0.560
SNRNP70	GTPBP1	psi-mi:“MI:0914”(association)	0.530
MAGEB2	POLRMT	psi-mi:“MI:0914”(association)	0.530
LUC7L2	CASC3	psi-mi:“MI:0914”(association)	0.530
RBM34	NVL	psi-mi:“MI:0914”(association)	0.530
SRPK2	RRP9	psi-mi:“MI:0914”(association)	0.530
SRPK1	DROSHA	psi-mi:“MI:0914”(association)	0.530
HDGFL2	CDC7	psi-mi:“MI:0914”(association)	0.530
RBMX2	WDR46	psi-mi:“MI:0914”(association)	0.530

BioGRID (656): CHTOP (Affinity Capture-MS), YBX3 (Affinity Capture-MS), DDX5 (Affinity Capture-MS), EWSR1 (Affinity Capture-MS), FUS (Affinity Capture-MS), HNRNPM (Affinity Capture-MS), ILF3 (Affinity Capture-MS), RPL37 (Affinity Capture-MS), SRRM2 (Affinity Capture-MS), ALYREF (Affinity Capture-MS), WIBG (Affinity Capture-MS), TP53 (Two-hybrid), SAFB (Two-hybrid), SRPK1 (Reconstituted Complex), SRPK1 (Affinity Capture-Western)

ESM2 similar proteins: A0AUV4, A0JM98, A1A5Q6, A2KF29, B1WAS2, C0HKC8, C0HKC9, O60285, O70551, O88866, P51957, P57058, P57059, Q2T9U5, Q4R9F7, Q5R7G9, Q5RD27, Q5REX1, Q5XHI9, Q60670, Q641K5, Q66HE5, Q68UT7, Q6IFT4, Q6P3R8, Q6REY9, Q6VZ17, Q80VH0, Q8BI55, Q8BLD6, Q8BZN4, Q8C0N0, Q8C0V7, Q8C0X8, Q8CFH6, Q8NE63, Q8TF76, Q96SB4, Q9H093, Q9H0K1

Diamond homologs: B0Y8Y4, B8Y466, O54781, O70551, P78362, Q03563, Q45FA5, Q4WW94, Q5RD27, Q5UQ24, Q61IS6, Q93VK0, Q96SB4, Q9UPE1, Q9Z0G2, A0A509AHB6, A8WJR8, B2MVY4, E2RTQ7, G5EBT1, G5EDB2, O35492, O35493, O43781, O59853, O76039, O93982, P11802, P14680, P14681, P30285, P32350, P35426, P36616, P46551, P49657, P49761, P51137, P51566, P51568

SIGNOR signaling

8 interactions.

A	Effect	B	Mechanism
SRPK1	down-regulates	RBM8A	phosphorylation
SRPK1	up-regulates	SRPK1	phosphorylation
LIMK2	“up-regulates activity”	SRPK1	phosphorylation
SRPK1	“up-regulates activity”	ARSF	phosphorylation
SRPK1	up-regulates	SRSF1	phosphorylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 218 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

Pathway	Partners	Fold	FDR
Metabolism of non-coding RNA	5	20.3×	7e-05
Transport of Mature Transcript to Cytoplasm	7	17.1×	3e-06
RNA Polymerase II Transcription Termination	12	16.9×	3e-10
mRNA 3’-end processing	13	16.4×	8e-11
SARS-CoV-2 modulates host translation machinery	10	14.3×	4e-08
mRNA Polyadenylation	25	14.1×	1e-19
mRNA Splicing	20	14.1×	1e-15
mRNA Splicing - Minor Pathway	9	12.9×	6e-07

GO biological processes:

GO term	Partners	Fold	FDR
negative regulation of mRNA splicing, via spliceosome	8	31.4×	2e-08
mRNA splice site recognition	7	28.8×	4e-07
spliceosomal complex assembly	8	24.7×	1e-07
regulation of mRNA splicing, via spliceosome	5	22.7×	2e-04
spliceosomal snRNP assembly	7	20.9×	4e-06
U2-type prespliceosome assembly	6	19.2×	5e-05
cytoplasmic translation	17	16.1×	2e-13
RNA splicing, via transesterification reactions	5	16.0×	9e-04

Disease & clinical

Clinical variants and AI predictions

ClinVar

83 variants total. Per-class counts are floors (≥ shown; pagination cap):

Classification	Count (floor)
Pathogenic	0
Likely pathogenic	0
Uncertain significance	62
Likely benign	0
Benign	1

Top pathogenic / likely-pathogenic (0)

SpliceAI

2647 predictions. Top by Δscore:

Variant	Effect	Δscore
6:35842530:CTCA:C	donor_loss	1.0000
6:35842531:TCACC:T	donor_loss	1.0000
6:35842532:CACCT:C	donor_loss	1.0000
6:35842533:A:AT	donor_loss	1.0000
6:35842534:C:A	donor_loss	1.0000
6:35842602:GGCC:G	acceptor_loss	1.0000
6:35842603:GCC:G	acceptor_loss	1.0000
6:35842604:CCTAA:C	acceptor_loss	1.0000
6:35842605:C:CC	acceptor_gain	1.0000
6:35842605:CTAAA:C	acceptor_loss	1.0000
6:35842606:T:A	acceptor_loss	1.0000
6:35857364:TTGTG:T	acceptor_gain	1.0000
6:35857369:C:CC	acceptor_gain	1.0000
6:35869003:AACTT:A	donor_loss	1.0000
6:35869004:ACTT:A	donor_loss	1.0000
6:35869005:CTTAC:C	donor_loss	1.0000
6:35869006:TTA:T	donor_loss	1.0000
6:35869007:TACCA:T	donor_loss	1.0000
6:35869008:A:AT	donor_loss	1.0000
6:35869008:ACCAC:A	donor_gain	1.0000
6:35869009:CCA:C	donor_gain	1.0000
6:35869009:CCACC:C	donor_gain	1.0000
6:35870956:CTGA:C	acceptor_gain	1.0000
6:35870957:TGA:T	acceptor_gain	1.0000
6:35870960:C:CC	acceptor_gain	1.0000
6:35886734:AACT:A	donor_gain	1.0000
6:35888015:AATAC:A	donor_loss	1.0000
6:35888016:ATAC:A	donor_loss	1.0000
6:35888017:TAC:T	donor_loss	1.0000
6:35888018:AC:A	donor_loss	1.0000

AlphaMissense

4329 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
6:35835341:G:T	A644D	1.000
6:35835349:T:A	R641S	1.000
6:35835349:T:G	R641S	1.000
6:35835350:C:G	R641T	1.000
6:35835395:A:G	F626S	1.000
6:35835420:A:G	W618R	1.000
6:35835420:A:T	W618R	1.000
6:35835427:C:A	K615N	1.000
6:35835427:C:G	K615N	1.000
6:35835437:A:G	L612P	1.000
6:35835437:A:T	L612Q	1.000
6:35835454:C:A	W606C	1.000
6:35835454:C:G	W606C	1.000
6:35835456:A:G	W606R	1.000
6:35835456:A:T	W606R	1.000
6:35835473:A:C	I600S	1.000
6:35835473:A:G	I600T	1.000
6:35835473:A:T	I600N	1.000
6:35835482:A:G	L597P	1.000
6:35835482:A:T	L597Q	1.000
6:35838405:A:G	L572P	1.000
6:35838407:T:A	E571D	1.000
6:35838407:T:G	E571D	1.000
6:35838408:T:A	E571V	1.000
6:35838409:C:T	E571K	1.000
6:35838420:G:T	A567E	1.000
6:35838426:T:G	H565P	1.000
6:35838427:G:C	H565D	1.000
6:35838428:A:C	D564E	1.000
6:35838428:A:T	D564E	1.000

dbSNP variants (sampled 300 via entrez): RS1000018594 (6:35854553 C>T), RS1000067290 (6:35867085 G>A), RS1000085400 (6:35905575 A>G), RS1000155573 (6:35850058 G>T), RS1000171513 (6:35851504 A>G), RS1000205613 (6:35848290 C>T), RS1000219672 (6:35854826 T>G), RS1000225752 (6:35893112 T>C), RS1000303821 (6:35915917 A>C), RS1000339316 (6:35836574 G>A), RS1000372448 (6:35886150 G>A), RS1000376761 (6:35841808 G>C), RS1000380871 (6:35911668 C>A), RS1000473893 (6:35880590 T>A,C), RS1000506677 (6:35900995 A>T)

Disease associations

OMIM: gene MIM:601939 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

0 total (0 of 0 shown, HPO-id order):

GWAS associations

4 associations (top):

Study	Trait	p-value
GCST007355_3	Antidepressant treatment resistance (> 2 drugs prescribed)	4.000000e-07
GCST90002390_576	Mean corpuscular hemoglobin	2.000000e-35
GCST90002392_753	Mean corpuscular volume	5.000000e-34
GCST90002396_282	Mean reticulocyte volume	5.000000e-15

EFO canonical traits (2, from GWAS)

EFO ID	Trait name
EFO:0004527	mean corpuscular hemoglobin
EFO:0010701	mean reticulocyte volume

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL4375 (SINGLE PROTEIN)

Molecules with ChEMBL bioactivity

24 molecules (phase ≥1), by development phase (incl. off-target/promiscuous compounds). Patent mentions across the top 20 by phase: 254,269 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

Molecule	Name	Phase	Patents
CHEMBL1287853	FEDRATINIB	4	3,554
CHEMBL1289926	AXITINIB	4	15,732
CHEMBL1336	SORAFENIB	4	86,060
CHEMBL1738797	ALECTINIB	4	6,731
CHEMBL1789941	RUXOLITINIB	4	11,547
CHEMBL502835	NINTEDANIB	4	8,545
CHEMBL535	SUNITINIB	4	79,020
CHEMBL576982	QUIZARTINIB	4	4,432
CHEMBL601719	CRIZOTINIB	4	14,403
CHEMBL608533	MIDOSTAURIN	4	7,259
CHEMBL223360	LINIFANIB	3	3,925
CHEMBL483158	ALISERTIB	3	2,305
CHEMBL522892	DOVITINIB	3	4,944
CHEMBL603469	LESTAURTINIB	3
CHEMBL91829	RUBOXISTAURIN	3	77
CHEMBL1721885	SU-014813	2	363
CHEMBL230011	TG100-115	2	1,504
CHEMBL362558	LY-2090314	2	108
CHEMBL475251	R-406	2	762
CHEMBL572878	TOZASERTIB	2	2,998
CHEMBL1084546	PF-00562271	1
CHEMBL1908397	KW-2449	1
CHEMBL1980391	RG-1530	1
CHEMBL482767	SNS-314	1

PharmGKB: 1 entry (VIP=true, CPIC=false)

GtoPdb / IUPHAR curated pharmacology

(IUPHAR/BPS Guide to Pharmacology — expert-curated)

Target class: enzyme — SRPK family

Most potent curated ligand interactions (1 total), top 1:

Ligand	Action	Affinity	Parameter
compound 13 [PMID: 15925511]	Inhibition	7.4	pIC50

Binding affinities (BindingDB)

46 measured of 47 human assays (47 total across all organisms); most potent 46 below. Values come from heterogeneous assays and are not directly comparable.

Ligand	Measure	Value	Patent
Staurosporine	KD	1.7 nM
5-methyl-N-[2-[4-[(2-methylsulfanylpyrimidin-4-yl)methyl]piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	1.9 nM	US-9695160: Piperazine derivatives for treating disorders
5-(oxan-4-yl)-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	2.6 nM	US-9695160: Piperazine derivatives for treating disorders
N-[2-(4-benzylpiperazin-1-yl)-5-(trifluoromethyl)phenyl]-5-methylfuran-2-carboxamide	IC50	4.4 nM	US-9695160: Piperazine derivatives for treating disorders
N-[2-(4-benzylpiperazin-1-yl)-5-(trifluoromethyl)phenyl]-5-pyridin-3-ylfuran-2-carboxamide	IC50	4.6 nM	US-9695160: Piperazine derivatives for treating disorders
5-[3-(hydroxymethyl)phenyl]-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	5 nM	US-9695160: Piperazine derivatives for treating disorders
5-pyridin-4-yl-N-[2-[4-(pyridin-4-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	7.18 nM	US-9695160: Piperazine derivatives for treating disorders
5-pyridin-3-yl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	13.5 nM	US-9796707: Piperazine derivatives for treating disorders
5-(1H-indol-5-yl)-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	13.9 nM	US-9796707: Piperazine derivatives for treating disorders
N-[2-(4-benzylpiperazin-1-yl)-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	14 nM	US-9695160: Piperazine derivatives for treating disorders
N-[2-(4-benzylpiperazin-1-yl)-5-(trifluoromethyl)phenyl]-5-pyridin-4-ylfuran-2-carboxamide	IC50	14.8 nM	US-9796707: Piperazine derivatives for treating disorders
N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	16.6 nM	US-9796707: Piperazine derivatives for treating disorders
5-pyridin-4-yl-N-[2-[4-(pyridin-3-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	17 nM	US-9695160: Piperazine derivatives for treating disorders
SPHINX scaffold, 2	IC50	20 nM
SPHINX scaffold, 1	IC50	31 nM
SPHINX scaffold, 3	IC50	36 nM
5-methyl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	38 nM	US-9695160: Piperazine derivatives for treating disorders
5-phenyl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	111 nM	US-9695160: Piperazine derivatives for treating disorders
5-(hydroxymethyl)-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	119 nM	US-9695160: Piperazine derivatives for treating disorders
N-[2-[4-(1H-indol-3-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]-5-pyridin-4-ylfuran-2-carboxamide	IC50	164 nM	US-9695160: Piperazine derivatives for treating disorders
5-(2-methoxy-4-pyridinyl)-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	170 nM	US-9695160: Piperazine derivatives for treating disorders
N-[2-[4-(pyrazin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	183 nM	US-9695160: Piperazine derivatives for treating disorders
PKC-412	KD	190 nM
SPHINX31	IC50	300 nM
5-(6-methoxy-3-pyridinyl)-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	IC50	323 nM	US-9695160: Piperazine derivatives for treating disorders
N-[2-[4-[(4-methoxyphenyl)methyl]piperazin-1-yl]-5-(trifluoromethyl)phenyl]-5-pyridin-4-ylfuran-2-carboxamide	IC50	336 nM	US-9695160: Piperazine derivatives for treating disorders
SPHINX	IC50	440 nM	US-9695160: Piperazine derivatives for treating disorders
N-[2-(4-methylpiperazin-1-yl)-5-(trifluoromethyl)phenyl]-5-phenyl-1H-imidazole-2-carboxamide	IC50	493 nM	US-9695160: Piperazine derivatives for treating disorders
(3Z)-4-amino-5-fluoro-3-[5-(4-methylpiperazino)-1,3-dihydrobenzimidazol-2-ylidene]carbostyril	KD	520 nM
N-[4-({4-[(3-methyl-1H-pyrazol-5-yl)amino]-6-(4-methylpiperazin-1-yl)pyrimidin-2-yl}sulfanyl)phenyl]cyclopropanecarboxamide	KD	1100 nM
N-[2-[4-[(3-methoxyphenyl)methyl]piperazin-1-yl]-5-(trifluoromethyl)phenyl]-5-pyridin-4-ylfuran-2-carboxamide	IC50	1550 nM	US-9695160: Piperazine derivatives for treating disorders
5-[(Z)-(5-fluoranyl-2-oxidanylidene-1H-indol-3-ylidene)methyl]-2,4-dimethyl-N-[(2S)-3-morpholin-4-yl-2-oxidanyl-propyl]-1H-pyrrole-3-carboxamide	KD	2600 nM
1-Acyl-1H-[1,2,4]triazole-3,5-diamine Analogue 3b	KD	3100 nM
N-[2-(diethylamino)ethyl]-5-[(Z)-(5-fluoro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carboxamide	KD	3500 nM
N-[2-(4-benzylpiperazin-1-yl)-5-(trifluoromethyl)phenyl]-5-(1H-indol-5-yl)furan-2-carboxamide	IC50	3510 nM	US-9695160: Piperazine derivatives for treating disorders
N-[2-(4-benzylpiperazin-1-yl)-5-(trifluoromethyl)phenyl]-5-phenylfuran-2-carboxamide	IC50	4010 nM	US-9695160: Piperazine derivatives for treating disorders
2-phenyl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]-1,3-oxazole-5-carboxamide	IC50	4030 nM	US-9695160: Piperazine derivatives for treating disorders
N-[2-(4-methylpiperazin-1-yl)-5-(trifluoromethyl)phenyl]thiophene-2-carboxamide	IC50	4690 nM	US-9695160: Piperazine derivatives for treating disorders
3-phenyl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]-1,2,4-oxadiazole-5-carboxamide	IC50	5310 nM	US-9695160: Piperazine derivatives for treating disorders
N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]-1H-1,2,4-triazole-5-carboxamide	IC50	8410 nM	US-9695160: Piperazine derivatives for treating disorders
5-phenyl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]-1,3,4-oxadiazole-2-carboxamide	IC50	10000 nM	US-9695160: Piperazine derivatives for treating disorders
5-methyl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]-1,3-oxazole-2-carboxamide	IC50	10000 nM	US-9695160: Piperazine derivatives for treating disorders
5-methyl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]-1,3,4-oxadiazole-2-carboxamide	IC50	10000 nM	US-9695160: Piperazine derivatives for treating disorders
5-pyridin-4-yl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]-1,3,4-oxadiazole-2-carboxamide	IC50	10000 nM	US-9695160: Piperazine derivatives for treating disorders
5-phenyl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]-1,2,4-oxadiazole-3-carboxamide	IC50	10000 nM	US-9695160: Piperazine derivatives for treating disorders
5-pyridin-4-yl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]-1,2,4-oxadiazole-3-carboxamide	IC50	10000 nM	US-9796707: Piperazine derivatives for treating disorders

ChEMBL bioactivities

451 potent at pChembl≥5 of 455 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChembl	Type	Value	Unit	Molecule
9.43	IC50	0.37	nM	CHEMBL5930435
9.30	IC50	0.5	nM	CHEMBL5965082
9.30	IC50	0.5	nM	CHEMBL6029449
9.15	IC50	0.7	nM	CHEMBL5934367
9.12	IC50	0.76	nM	CHEMBL5917789
9.05	IC50	0.884	nM	CHEMBL3747611
8.94	IC50	1.15	nM	CHEMBL3747134
8.94	IC50	1.15	nM	CHEMBL6170692
8.92	IC50	1.2	nM	CHEMBL5909482
8.89	IC50	1.3	nM	CHEMBL5990226
8.85	IC50	1.4	nM	CHEMBL6018331
8.78	IC50	1.68	nM	CHEMBL4468747
8.77	IC50	1.7	nM	CHEMBL5811732
8.74	IC50	1.8	nM	CHEMBL5906376
8.74	IC50	1.8	nM	CHEMBL5750651
8.72	IC50	1.9	nM	CHEMBL5894352
8.72	IC50	1.91	nM	CHEMBL3746522
8.60	IC50	2.53	nM	CHEMBL3747301
8.59	IC50	2.6	nM	CHEMBL5918528
8.58	IC50	2.61	nM	CHEMBL3746627
8.57	IC50	2.7	nM	CHEMBL5085558
8.57	IC50	2.66	nM	CHEMBL3746960
8.55	IC50	2.8	nM	CHEMBL6018983
8.52	IC50	3	nM	CHEMBL5085558
8.52	IC50	3.01	nM	CHEMBL3747406
8.50	IC50	3.18	nM	CHEMBL5074274
8.46	IC50	3.5	nM	CHEMBL5996135
8.43	IC50	3.7	nM	CHEMBL6031872
8.36	IC50	4.4	nM	CHEMBL5908237
8.34	IC50	4.6	nM	CHEMBL5878480
8.34	IC50	4.6	nM	CHEMBL5856679
8.32	IC50	4.75	nM	CHEMBL3747108
8.30	IC50	5	nM	CHEMBL5749164
8.29	IC50	5.09	nM	CHEMBL3746395
8.28	IC50	5.3	nM	CHEMBL6029175
8.26	IC50	5.5	nM	CHEMBL5847882
8.26	Kd	5.5	nM	STAUROSPORINE
8.22	IC50	6	nM	CHEMBL5074274
8.17	IC50	6.7	nM	CHEMBL5930064
8.15	IC50	7	nM	CHEMBL5439515
8.14	IC50	7.18	nM	CHEMBL5904988
8.09	IC50	8.2	nM	CHEMBL5755331
8.06	IC50	8.8	nM	CHEMBL5996933
8.01	IC50	9.7	nM	CHEMBL5782913
8.00	Kd	10	nM	LESTAURTINIB
7.97	IC50	10.7	nM	CHEMBL5803127
7.96	IC50	10.9	nM	CHEMBL5748071
7.96	IC50	11	nM	ALECTINIB
7.95	IC50	11.3	nM	CHEMBL5906195
7.90	IC50	12.7	nM	CHEMBL5893054

PubChem BioAssay actives

94 with measured affinity, of 1598 total; 50 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

Compound	Assay	Type	Value	Unit
3-(3-cyano-9-ethyl-6,6-dimethyl-11-oxo-5H-benzo[b]carbazol-8-yl)benzenesulfonyl fluoride	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0017	uM
N-[3-[[[2-(5-chloro-4-fluoro-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0030	uM
(2S,3R,4R,6R)-3-methoxy-2-methyl-4-(methylamino)-29-oxa-1,7,17-triazaoctacyclo[12.12.2.12,6.07,28.08,13.015,19.020,27.021,26]nonacosa-8,10,12,14,19,21,23,25,27-nonaen-16-one	435936: Binding constant for full-length SRPK1	kd	0.0055	uM
5-pyridin-4-yl-N-[2-[4-(pyridin-2-ylmethyl)piperazin-1-yl]-5-(trifluoromethyl)phenyl]furan-2-carboxamide	1802550: In Vitro Kinase Screening Assay from Article 10.1021/acschembio.6b01048: “Development of Potent, Selective SRPK1 Inhibitors as Potential Topical Therapeutics for Neovascular Eye Disease.”	ic50	0.0059	uM
N-[3-[[[2-(6-chloro-4-fluoro-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0070	uM
(15S,16S,18R)-16-hydroxy-16-(hydroxymethyl)-15-methyl-28-oxa-4,14,19-triazaoctacyclo[12.11.2.115,18.02,6.07,27.08,13.019,26.020,25]octacosa-1,6,8,10,12,20,22,24,26-nonaen-3-one	508091: Binding affinity to SRPK1	kd	0.0100	uM
5-methyl-N-[2-morpholin-4-yl-5-(trifluoromethyl)phenyl]furan-2-carboxamide	1851164: Inhibition of SRPK1 (unknown origin) using SRSF1 Arg-Ser (RS) peptide (NH2-RSPSYGRSRSRSRSRSRSRSRSNSRSRSY-OH) as substrate incubated for 10 mins in presence of ATP by Kinase-Glo assay	ic50	0.0100	uM
N-[3-[[[6-(6-chloro-1H-benzimidazol-2-yl)-2-pyridinyl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0150	uM
N-[3-[[2-(6-chloro-1H-benzimidazol-2-yl)pyrrolo[2,3-d]pyrimidin-7-yl]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0150	uM
N-[3-[[[5-bromo-2-(6-chloro-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0160	uM
N-[3-[[[2-(4,6-difluoro-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0180	uM
N-[2-(4-methylpiperazin-1-yl)-5-(trifluoromethyl)phenyl]-5-pyridin-4-ylfuran-2-carboxamide	1802548: In Vitro Kinase Screening Assay from Article 10.1021/acschembio.6b01048: “Development of Potent, Selective SRPK1 Inhibitors as Potential Topical Therapeutics for Neovascular Eye Disease.”	ic50	0.0200	uM
N-[3-[[[2-(4-chloro-6-fluoro-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0220	uM
N-[3-[[[2-(6-chloro-1H-benzimidazol-2-yl)pyrimidin-4-yl]-methylamino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0240	uM
N-[3-[[[2-(5,6-difluoro-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0240	uM
5-methyl-N-[2-(4-methylpiperazin-1-yl)-5-(trifluoromethyl)phenyl]furan-2-carboxamide	1802548: In Vitro Kinase Screening Assay from Article 10.1021/acschembio.6b01048: “Development of Potent, Selective SRPK1 Inhibitors as Potential Topical Therapeutics for Neovascular Eye Disease.”	ic50	0.0310	uM
N-methyl-N-[3-[[[2-[6-(1-methylpyrazol-4-yl)-1H-benzimidazol-2-yl]pyrimidin-4-yl]amino]methyl]-2-pyridinyl]methanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0310	uM
N-[3-[[[2-(5-chloro-6-fluoro-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0320	uM
N-[3-[[[2-(6-chloro-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0320	uM
N-[3-[[2-(6-chloro-1H-benzimidazol-2-yl)-6-methylpyrrolo[2,3-d]pyrimidin-7-yl]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0350	uM
N-methyl-N-[3-[[[2-(6-propan-2-yl-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]methanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0360	uM
methyl 2-hydroxy-3-[N-[4-[methyl-[2-(4-methylpiperazin-1-yl)acetyl]amino]phenyl]-C-phenylcarbonimidoyl]-1H-indole-6-carboxylate	624903: Binding constant for SRPK1 kinase domain	kd	0.0370	uM
2,3-dithiophen-2-ylbenzo[g]quinoxaline-7-carboxylic acid	1188117: Inhibition of SRPK1 kinase (unknown origin)	ic50	0.0400	uM
(3Z)-5-[(2,6-dichlorophenyl)methylsulfonyl]-3-[[3,5-dimethyl-4-[(2R)-2-(pyrrolidin-1-ylmethyl)pyrrolidine-1-carbonyl]-1H-pyrrol-2-yl]methylidene]-1H-indol-2-one	624903: Binding constant for SRPK1 kinase domain	kd	0.0410	uM
Midostaurin	435936: Binding constant for full-length SRPK1	kd	0.0420	uM
N-[3-[[[2-(6-chloro-4-fluoro-1H-benzimidazol-2-yl)pyrimidin-5-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1956444: Inhibition of SRPK1 (unknown origin) using RS peptide as substrate incubated for 120 mins in the presence 33P-ATP	ic50	0.0500	uM
N-[3-[[[2-(4,6-difluoro-1H-benzimidazol-2-yl)pyrimidin-5-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1956444: Inhibition of SRPK1 (unknown origin) using RS peptide as substrate incubated for 120 mins in the presence 33P-ATP	ic50	0.0500	uM
N-methyl-N-[3-[[[2-(6-methyl-1H-benzimidazol-2-yl)pyrimidin-5-yl]amino]methyl]-2-pyridinyl]methanesulfonamide	1956444: Inhibition of SRPK1 (unknown origin) using RS peptide as substrate incubated for 120 mins in the presence 33P-ATP	ic50	0.0500	uM
N-[3-[[[6-(6-chloro-1H-benzimidazol-2-yl)-3-pyridinyl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1956444: Inhibition of SRPK1 (unknown origin) using RS peptide as substrate incubated for 120 mins in the presence 33P-ATP	ic50	0.0500	uM
N-methyl-N-[3-[[[2-[6-(1-methylpyrazol-4-yl)-1H-benzimidazol-2-yl]pyrimidin-5-yl]amino]methyl]-2-pyridinyl]methanesulfonamide	1956444: Inhibition of SRPK1 (unknown origin) using RS peptide as substrate incubated for 120 mins in the presence 33P-ATP	ic50	0.0500	uM
N-methyl-N-[3-[[[2-(6-propan-2-yl-1H-benzimidazol-2-yl)pyrimidin-5-yl]amino]methyl]-2-pyridinyl]methanesulfonamide	1956444: Inhibition of SRPK1 (unknown origin) using RS peptide as substrate incubated for 120 mins in the presence 33P-ATP	ic50	0.0500	uM
[4-[(E)-2-(1H-indazol-3-yl)ethenyl]phenyl]-piperazin-1-ylmethanone	624903: Binding constant for SRPK1 kinase domain	kd	0.0550	uM
N-[3-[[[2-(6-fluoro-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0580	uM
N-[2-[4-[2-(dimethylamino)ethyl]piperazin-1-yl]-5-(trifluoromethyl)phenyl]-5-pyridin-4-ylfuran-2-carboxamide	1802548: In Vitro Kinase Screening Assay from Article 10.1021/acschembio.6b01048: “Development of Potent, Selective SRPK1 Inhibitors as Potential Topical Therapeutics for Neovascular Eye Disease.”	ic50	0.0590	uM
N-[3-[[[2-(5-chloro-1-methylbenzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0650	uM
N-[3-[[[2-[6-fluoro-5-(4-methylpiperazin-1-yl)-1H-benzimidazol-2-yl]pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0810	uM
N-[4-[4-(4-methylpiperazin-1-yl)-6-[(5-methyl-1H-pyrazol-3-yl)amino]pyrimidin-2-yl]sulfanylphenyl]cyclopropanecarboxamide	435936: Binding constant for full-length SRPK1	kd	0.0820	uM
N-[2-piperidin-1-yl-5-(trifluoromethyl)phenyl]pyridine-4-carboxamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.0830	uM
N-[3-[[6-(6-chloro-1H-benzimidazol-2-yl)pyrrolo[3,2-c]pyridin-1-yl]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.1070	uM
N-[(1R,2S)-2-aminocyclohexyl]-4-[6-(1-methylpyrazol-4-yl)pyrazolo[1,5-a]pyrimidin-3-yl]thiophene-2-carboxamide	1637138: Inhibition of full-length recombinant human His-tagged SRPK1 expressed in baculovirus expression system by Z’-LYTE assay	ic50	0.1400	uM
N-[3-[[[2-(6-methoxy-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.1520	uM
Fedratinib	624903: Binding constant for SRPK1 kinase domain	kd	0.1600	uM
N-methyl-N-[3-[[[2-(6-methyl-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]methanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.1640	uM
Alectinib	1553484: Inhibition of SRPK1 (unknown origin) by TR-FRET assay	ic50	0.1950	uM
Sunitinib	435936: Binding constant for full-length SRPK1	kd	0.2500	uM
N-[3-[[[2-(6-cyano-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.3240	uM
N-methyl-N-[3-[[[2-(6-morpholin-4-yl-1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]methanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.3570	uM
(3Z)-3-(1H-pyrrol-2-ylmethylidene)-1H-indol-2-one	389044: Binding affinity to human SRPK1	kd	0.3610	uM
4-amino-5-fluoro-3-[6-(4-methylpiperazin-1-yl)-1H-benzimidazol-2-yl]-1H-quinolin-2-one	435936: Binding constant for full-length SRPK1	kd	0.4200	uM
N-[3-[[[2-(1H-benzimidazol-2-yl)pyrimidin-4-yl]amino]methyl]-2-pyridinyl]-N-methylmethanesulfonamide	1968975: Inhibition of human SRPK1 using GRSRSRSRSR as substrate in presence of [gamma-33p]-ATP by radiometric hotspot kinase assay	ic50	0.4480	uM

CTD chemical–gene interactions

52 total (human), top 30 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
sodium arsenite	increases abundance, increases expression, decreases expression, affects cotreatment	3
bisphenol A	decreases expression	2
Estradiol	affects cotreatment, increases expression	2
7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide	decreases expression	2
FR900359	affects phosphorylation	1
2,4,6-tribromophenol	decreases expression	1
triphenyl phosphate	affects expression	1
alpha-pinene	affects cotreatment, decreases expression, increases oxidation, increases abundance	1
arsenite	affects binding, decreases reaction	1
manganese chloride	increases abundance, increases expression, affects cotreatment	1
methacrylaldehyde	affects cotreatment, decreases expression, increases oxidation, increases abundance	1
beta-methylcholine	affects expression	1
di-n-butylphosphoric acid	affects expression	1
CGP 52608	increases reaction, affects binding	1
pentabrominated diphenyl ether 100	decreases expression	1
hexabrominated diphenyl ether 153	decreases expression	1
1-(4-(6-bromobenzo(1,3)dioxol-5-yl)-3a,4,5,9b-tetrahydro-3H-cyclopenta(c)quinolin-8-yl)ethanone	increases phosphorylation	1
2-(1H-indazol-4-yl)-6-(4-methanesulfonylpiperazin-1-ylmethyl)-4-morpholin-4-ylthieno(3,2-d)pyrimidine	decreases expression, increases response to substance	1
Oxaliplatin	increases expression, affects response to substance	1
Resveratrol	decreases expression	1
Norethindrone Acetate	affects cotreatment, increases expression	1
Acrolein	affects cotreatment, decreases expression, increases oxidation, increases abundance	1
Air Pollutants	affects cotreatment, decreases expression, increases abundance, increases oxidation	1
Arsenic	increases expression, affects cotreatment, increases abundance	1
Benzo(a)pyrene	increases expression, affects cotreatment	1
Biological Factors	decreases activity, increases secretion	1
Cadmium	increases expression	1
Caffeine	decreases phosphorylation	1
Calcitriol	decreases expression	1
Cisplatin	affects localization	1

ChEMBL screening assays

374 unique, capped per target: 373 binding, 1 functional

Representative assays (with source publication via chembl_document):

Assay ID	Type	Description	Source paper
CHEMBL1003338	Binding	Inhibition of SRPK1 at 1 uM relative to control	Novel potent BRAF inhibitors: toward 1 nM compounds through optimization of the central phenyl ring. — J Med Chem
CHEMBL1963724	Functional	PUBCHEM_BIOASSAY: Navigating the Kinome. (Class of assay: other) Panel member name: SRPK1	PubChem BioAssay data set

Cellosaurus cell lines

7 cell lines: 5 cancer cell line, 2 hybrid cell line

First 10 cell lines (id-ordered, not curated):

Cellosaurus	Name	Category	Sex
CVCL_B7ZL	Abcam Raji SRPK1 KO	Cancer cell line	Male
CVCL_C0AE	Abcam THP-1 SRPK1 KO	Cancer cell line	Male
CVCL_C7C2	Abcam PC-3 SRPK1 KO	Cancer cell line	Male
CVCL_TQ46	HAP1 SRPK1 (-) 1	Cancer cell line	Male
CVCL_TQ47	HAP1 SRPK1 (-) 2	Cancer cell line	Male
CVCL_YT53	CNE1 SRPK1 KO	Hybrid cell line
CVCL_YT55	CNE1 SRPK1/2 KO	Hybrid cell line

Clinical trials (associated diseases)

0 trials via MONDO — disease-level, not drug-specific.